PHPT1 Human

The discovery of protein phosphorylation on histidine dates back over five decades . Historically, most research on phosphohistidine has focused on bacterial systems, such as the phosphoenolpyruvate-glucose phosphotransferase system and two-component systems . In eukaryotic cells, protein-bound phosphohistidine constitutes a significant portion of the total phosphoamino acids . However, the number of identified phosphohistidine-containing proteins is relatively low compared to those phosphorylated on serine, threonine, and tyrosine .

PHPT1 is known for its ability to dephosphorylate phosphohistidine-containing peptides and proteins . Interestingly, recent studies have shown that PHPT1 can also dephosphorylate phospholysine in chemically phosphorylated histone H1 and polylysine . This broader specificity highlights the enzyme’s versatility and importance in cellular processes .

The dephosphorylation activity of PHPT1 involves the removal of phosphate groups from histidine residues in proteins and peptides . This process is essential for regulating various cellular functions, including signal transduction, metabolic pathways, and enzyme activity . The enzyme’s activity has been studied using various techniques, such as DEAE-Sepharose spin column and mass spectrometry .

PHPT1 is associated with several diseases, including hemolytic disease of the fetus and newborn (Rh-induced) and immunodeficiency 18 . The enzyme’s role in these conditions underscores its importance in maintaining cellular homeostasis and proper physiological function .

Recombinant human PHPT1 has been extensively studied to understand its biochemical properties and potential therapeutic applications . The enzyme’s ability to dephosphorylate a wide range of substrates makes it a valuable tool for investigating protein phosphorylation and dephosphorylation mechanisms .

In conclusion, Phosphohistidine Phosphatase 1 (Human Recombinant) is a versatile and essential enzyme involved in the dephosphorylation of histidine-phosphorylated proteins and peptides. Its broader specificity and clinical significance make it a critical subject of ongoing research in the field of biochemistry and molecular biology.